Novel proliferative effect of phospholipase A2 in Swiss 3T3 cells via specific binding site

Hitoshi Arita, Kohji Hanasaki, Tohru Nakano, Shogo Oka, Hiroshi Teraoka, Koichi Matsumoto

研究成果: ジャーナルへの寄稿学術論文査読

172 被引用数 (Scopus)

抄録

Phospholipase A2 (PLA2), EC 3.1.1.4, which catalyzes the release of free fatty acids from the sn-2 position of glycerophospholipids, has been extensively studied from the viewpoint of eicosanoid Reduction (Arita, H., Nakano, T., and Hanasaki, K. (1989) Prog. Lipid Res. 28, 273-301). Several lines of evidence suggest that extracellular PLA2 is pathophysiologically related to some disorders, including inflammation and hypersensitivity. Despite this, little is known of the precise mechanism of the pathological processes as well as their intrinsic correlation with dysfunction. Here, we report a novel PLA2 action on the proliferation of Swiss 3T3 fibroblasts via specific binding sites of approximately Mr 200,000. Pancreatic type PLA2 in the active form specifically recognized the sites and stimulated thymidine incorporation in DNA. Its inactive zymogen and other PLA2s from platelets, snake, and bee venoms showed much lesser activities. Although the physiological significance remains to be identified, our finding is the first to offer a new viewpoint on the effect of mammalian extracellular PLA2 on cellular function.

本文言語英語
ページ(範囲)19139-19141
ページ数3
ジャーナルJournal of Biological Chemistry
266
29
出版ステータス出版済み - 15-10-1991
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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